Mutational analysis and membrane topology of ComP, a quorum-sensing histidine kinase of Bacillus subtilis controlling competence development

被引:56
作者
Piazza, F [1 ]
Tortosa, P [1 ]
Dubnau, D [1 ]
机构
[1] Publ Hlth Res Inst City New York Inc, New York, NY 10016 USA
关键词
D O I
10.1128/JB.181.15.4540-4548.1999
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
ComP is a sensor histidine kinase of Bacillus subtilis required for the signal transduction pathway that initiates the development of competence for genetic transformation. It is believed that ComP senses the presence of ComX, a modified extracellular peptide pheromone, and donates a phosphate to ComA, thereby activating this transcription factor for binding to the srfA promoter. In the present study, fusions to the Escherichia coli proteins PhoA and LacZ and analysis of its susceptibility to the protease kallikrein were used to probe the membrane topology of ComP. These data suggest that ComP contains six or eight membrane-spanning segments and two large extracytoplasmic loops in its N-terminal membrane-associated domain. Deletions were introduced involving the large extracellular loops to explore the role of the N-terminal domain of ComP in signal transduction. The absence of the second loop conferred a phenotype in which ComP was active in the absence of ComX. The implications of these data are discussed.
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收藏
页码:4540 / 4548
页数:9
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